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目的：初步了解哺乳类细胞非定标性突变形成是否与以蛋白质磷酸化级联反应为主要形式的细胞信号传导通路有关；方法：采用［３２Ｐ］体内预标记及凝胶双向电泳方法差异显示甲基硝基亚硝胍（ＭＮＮＧ）处理组和对照组磷酸化蛋白，蛋白质免疫印迹杂交试验初步鉴定差异显示蛋白斑点性质；结果：在处理组发现两个与对照组不同的蛋白斑点，分子量分别在６８×１０３和４３×１０３附近，与抗酪氨酸磷酸化蛋白抗体未发生阳性反应；结论：根据差异显示蛋白斑点的分子量和印迹杂交试验结果，初步认为所见蛋白斑点可能为丝／苏氨酸磷酸化蛋白，且可能为丝裂原激活的蛋白激酶（ＭＡＰＫ）成员
OBJECTIVE: To understand whether the non-site-specific mutagenesis of mammalian cells is related to cell signal transduction pathway which is the main form of protein phosphorylation cascade reaction.Methods: [32P] in vivo pre-labeling and gel electrophoresis The differences between the two groups were statistically significant (P <0.05) .Conclusion: The protein spots of the differentially expressed proteins were identified by MNNG treatment and control group phosphorylation protein and protein immunoblotting. Results: Two protein spots different from the control group were found in the treatment group, 68 × 103 and 43 × 103, respectively, and no positive reaction with anti-tyrosine phosphorylated protein antibody.Conclusion: Based on the molecular weight of the differential display protein spots and the blot hybridization test results, Acid phosphorylates proteins, and may be members of the mitogen-activated protein kinase (MAPK)